Improvement of lactulose synthesis through optimization of reaction conditions with immobilized β-galactosidase

Yoon Seok Song, Young Joon Suh, Chulhwan Park, Seung Wook Kim

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Kluyveromyces lactisβ-galactosidase was immobilized on silica gels using a covalent bonding method. To improve lactulose synthesis using immobilized β-galactosidase, the optimal reaction conditions, such as lactose and fructose concentrations, pH and ionic strength of the buffer, loading amount of the enzyme and temperature, were determined. Lactulose synthesis using the immobilized β-galactosidase was markedly improved after optimization of the reaction conditions. When the lactulose synthesis was carried out at 47 °C using 40% (w/v) lactose, 20% (w/v) fructose and immobilized β-galactosidase of 12 U/ml in 50 mM sodium phosphate buffer at pH 7. 5, the lactulose concentration and specific productivity were 15. 80 g/l and 1. 32 mg/U·h, respectively. In addition, when the immobilized β-galactosidase was reused for lactulose synthesis, its catalytic activity retained 60. 5% after 10 reuses.

Original languageEnglish
Pages (from-to)160-165
Number of pages6
JournalKorean Journal of Chemical Engineering
Volume30
Issue number1
DOIs
Publication statusPublished - 2013 Jan 1

Fingerprint

Galactosidases
Lactulose
Fructose
Lactose
Buffers
Silica Gel
Silica gel
Ionic strength
Catalyst activity
Phosphates
Enzymes
Productivity
Sodium

Keywords

  • β-Galactosidase
  • Immobilization
  • Lactulose
  • Optimization
  • Transgalactosylation

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Improvement of lactulose synthesis through optimization of reaction conditions with immobilized β-galactosidase. / Song, Yoon Seok; Suh, Young Joon; Park, Chulhwan; Kim, Seung Wook.

In: Korean Journal of Chemical Engineering, Vol. 30, No. 1, 01.01.2013, p. 160-165.

Research output: Contribution to journalArticle

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AU - Suh, Young Joon

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AU - Kim, Seung Wook

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N2 - Kluyveromyces lactisβ-galactosidase was immobilized on silica gels using a covalent bonding method. To improve lactulose synthesis using immobilized β-galactosidase, the optimal reaction conditions, such as lactose and fructose concentrations, pH and ionic strength of the buffer, loading amount of the enzyme and temperature, were determined. Lactulose synthesis using the immobilized β-galactosidase was markedly improved after optimization of the reaction conditions. When the lactulose synthesis was carried out at 47 °C using 40% (w/v) lactose, 20% (w/v) fructose and immobilized β-galactosidase of 12 U/ml in 50 mM sodium phosphate buffer at pH 7. 5, the lactulose concentration and specific productivity were 15. 80 g/l and 1. 32 mg/U·h, respectively. In addition, when the immobilized β-galactosidase was reused for lactulose synthesis, its catalytic activity retained 60. 5% after 10 reuses.

AB - Kluyveromyces lactisβ-galactosidase was immobilized on silica gels using a covalent bonding method. To improve lactulose synthesis using immobilized β-galactosidase, the optimal reaction conditions, such as lactose and fructose concentrations, pH and ionic strength of the buffer, loading amount of the enzyme and temperature, were determined. Lactulose synthesis using the immobilized β-galactosidase was markedly improved after optimization of the reaction conditions. When the lactulose synthesis was carried out at 47 °C using 40% (w/v) lactose, 20% (w/v) fructose and immobilized β-galactosidase of 12 U/ml in 50 mM sodium phosphate buffer at pH 7. 5, the lactulose concentration and specific productivity were 15. 80 g/l and 1. 32 mg/U·h, respectively. In addition, when the immobilized β-galactosidase was reused for lactulose synthesis, its catalytic activity retained 60. 5% after 10 reuses.

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